HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 290/2/F335    most recent 00253.2005v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (3) Citing Articles via Google Scholar Google Scholar Articles by Harita, Y. Articles by Kawachi, H. Search for Related Content PubMed PubMed Citation Articles by Harita, Y. Articles by Kawachi, H.

Altered expression of junctional adhesion molecule 4 in injured podocytes

¹Department of Cell Biology, Institute of Nephrology, Niigata University Graduate School of Medical and Dental Sciences, Niigata; and ²Department of Pediatrics, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan

Submitted 20 June 2005 ; accepted in final form 18 August 2005

Recent investigations have revealed the importance of glomerular podocytes with its diaphragm as the major filtration barrier. Junctional adhesion molecule 4 (JAM4) has been identified as a protein that interacts with membrane-associated guanyl kinase inverted (MAGI)-1 and is reported to be expressed on podocytes. To elucidate the role of JAM4 on podocytes, we examined the expression of JAM4 and MAGI-1 in normal and two different proteinuric rat models: puromycin aminonucleoside (PAN) nephropathy and anti-nephrin antibody-induced (ANA) nephropathy, one model with and one without effacement of podocyte foot processes. JAM4 was detected by immunomicroscopy at the apical membrane of normal podocytes. JAM4 immunostaining was focally increased in the podocytes in PAN nephropathy but not in ANA nephropathy. In proteinuric podocytes, the expression of JAM4 was distinct from that of MAGI-1 or other slit diaphragm molecules such as nephrin and ZO-1. Close colocalization of JAM4 and ezrin was maintained in PAN nephropathy. By immunoelectron microscopy, the signals for JAM4 were detected at the free apical membrane of the podocytes with effaced foot processes. Studies with selective detergent extract revealed that the subcellular localization of JAM4 was altered in PAN nephropathy. Thus the altered expression of JAM4 appears to be associated with morphological changes in podocytes and can be a useful marker of injured podocytes. JAM4 may have a different role at the apical membrane besides the role as a junctional molecule and is likely associated with the unique structure of this epithelium.

podocyte; puromycin aminonucleoside nephropathy; foot process effacement; membrane-associated guanyl kinase inverted-1

This article has been cited by other articles:

				P. F. Bradfield, S. Nourshargh, M. Aurrand-Lions, and B. A. Imhof JAM Family and Related Proteins in Leukocyte Migration (Vestweber Series) Arterioscler. Thromb. Vasc. Biol., October 1, 2007; 27(10): 2104 - 2112. [Abstract] [Full Text] [PDF]

				G. Nagamatsu, M. Ohmura, T. Mizukami, I. Hamaguchi, S. Hirabayashi, S. Yoshida, Y. Hata, T. Suda, and K. Ohbo A CTX Family Cell Adhesion Molecule, JAM4, Is Expressed in Stem Cell and Progenitor Cell Populations of both Male Germ Cell and Hematopoietic Cell Lineages Mol. Cell. Biol., November 15, 2006; 26(22): 8498 - 8506. [Abstract] [Full Text] [PDF]